Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes
- Structures of Actinonin-bound Peptide Deformylases from Enterococcus faecalis and Streptococcus pyogenes
- 김국한; 이원규; 최경재; 김은경
- actinonin; antibacterial target; drug design; Enterococcus faecalis; peptide deformylase; Streptococcus
- Issue Date
- 한국응용생명화학회지; JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
- VOL 57, NO 5, 565-571
- Bacterial resistance to many existing antibiotics is a growing health concern worldwide. There is an urgent need to identify new antibiotics with unexploited modes of action. Peptide
deformylase (PDF) is an essential enzyme involved in N-terminal protein processing in eubacteria but not in higher organisms. Therefore, PDF is considered an attractive target for the development of novel antibiotics. Here, we report the structures of the PDFs from Enterococcus faecalis (EfPDF) and Streptococcus pyogenes (SpyPDF) complexed with actinonin at 1.4 and 2.1 Å resolutions, respectively. Actinonin, a naturally occurring, highly potent inhibitor, is bound tightly at the active site. The conformation of actinonin in the EfPDF and SpyPDF complexes was similar to those of all others. The detailed information from this study will facilitate the
development of novel antibacterial molecules.
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